Amino acids (2) Flashcards

1
Q

Polypeptide

A

Polypeptide is a polymer of amino acids joined by peptide bonds

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2
Q

Hydrophobic

A

Hydrophobic means it repels water or lacks an affinity of water

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3
Q

Hydrophilic

A

Hydrophilic means it is capable of interacting with water through H bonding

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4
Q

Conjugated protein

A

Conjugated protein is a compound , like haemoglobin, that is made up of a protein molecule and a non protein prosthetic group.

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5
Q

What happens in condensation reaction

A

In Condensation reactions, OH from carboxylic acid group combines with H of amine on second amino acid. The OH and H are removed and combine to form water, leaving behind a peptide bond between C and N. When 2 amino acids join like this they have formed a dipeptide molecule.

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6
Q

Roles of proteins

A

Proteins roles are: enzymes, antibodies, hormones, proteins that provide support for muscles and tissues, provide bases for DNA, transport stuff in blood, contractile fibres, actin and myosin.

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7
Q

What happens when proteins don’t fold correctly

A

Incorrect folding of proteins is responsible for a number of diseases such as Alzheimer’s, Parkinson’s and cystic fibrosis.

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8
Q

Where is the peptide link

A

The peptide link is where the hydroxide and H formed water so the C double bonded to O which is bonded to N bonded to H

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9
Q

Characteristics of fibrous proteins

A

Fibrous proteins are long (contain many amino acids)
Amino acid sequence is repetitive and polypeptide chains lie parallel to each other, allowing cross links to form.
No tertiary structure - stay as long chains
E.g keratin in hair, collagen in skin
Insoluble in water
Roles: structural and keratin

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10
Q

Globular protein attributes

A

Globular proteins fold into a 3D spherical shape.
Irregular non repetitive sequence of amino acid
E.g haemoglobin, insulin and enzymes
Soluble in water
Metabolic role, enzymes plasma proteins

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11
Q

Hydrophobic interactions

A

Hydrophobic interactions is when r groups that are non polar turn towards the protein, away from water

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12
Q

What is a proteins function dependent on

A

A proteins function is dependent on its shape, and a mutation may change the composition of a protein so it cannot fold correctly and therefore cannot carry out its function in the cell.
Also, a change in pH may denature enzymes and proteins, changing their shape.

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13
Q

Why does secondary structure form

A

Secondary structure forms when adjacent C=O and N-H groups interact with each other to form hydrogen bonds resulting in arrangement of polypeptides in alpha helix or beta pleated sheet.
The O of C=O is slightly negative and the H of N-H is slightly positive, which creates electrostatic attraction.

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14
Q

What makes the secondary structure stable

A

Each H bond is weak but the overall effect of many H bonds makes secondary structure quite stable.

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15
Q

What is structure of an amino acid

A

Structure of amino acid is:
Has a carboxyl group, containing carbon double bonded to an oxygen and single bonded to a hydroxide group. Amino acid features a central carbon which is single bonded to a hydrogen and an R group. has an amino group consisting of a single N bonded to 2 Cs

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